AMYR_DROPN
ID AMYR_DROPN Reviewed; 494 AA.
AC O77022;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-amylase-related protein;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE Flags: Precursor;
GN Name=Amyrel;
OS Drosophila punjabiensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=60717;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Da Lage J.-L.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; U96165; AAC39115.1; -; Genomic_DNA.
DR AlphaFoldDB; O77022; -.
DR SMR; O77022; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR FlyBase; FBgn0021218; Dpun\Amyrel.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..494
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001384"
FT ACT_SITE 208
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 206
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 308
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 343
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 48..104
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 157..171
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 376..382
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 418..441
FT /evidence="ECO:0000255"
FT DISULFID 448..460
FT /evidence="ECO:0000250|UniProtKB:P56634"
SQ SEQUENCE 494 AA; 55679 MW; 074E7C129C4805AC CRC64;
MFKFALALTL CLAGASLSLA QHNPQWWGNR NTIVHLFEWK WSDIAGECET FLAPRGFAGV
QVSPVNENII AAGRPWWERY QPISYKLTTR SGNEEEFADM VRRCNDVGIR IYVDVLLNHM
SGDFDGVAVG TAGTEAEPSK KSFPGVPHTA QDFHPSCEIT DWNDRFQVQE CELVGLKDLN
QHSDYVRSKL IEFLDHLIEL GVAGFRVDAA KHMAAEDLEY IYGSLSNLNI EHGFPHNARP
FIFQEVIDHG HETVSREEYN QLGAVTEFRF SEEIGRAFRG NNALKWLQSW GTDWGFLNSE
QALTFVDNHD NQRDHGSVLN YKSPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTPPPQD
AQENIISPEF DEDGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSGWWDN GDNQISFCRG
NKGFLAVNNN LYDLSQELNT CLPAGEYCDV ISGSLIDGAC TGKSVTVNEY GYGYIHIGSD
DFDGVLALHV NAKV
